| Accepted Name |
|---|
| bacterial tyrosine kinase
|
| Alternative Name(s) |
|---|
| bacterial protein tyrosine kinase |
| BY-kinase |
| Reaction catalysed |
|---|
| L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+) |
| Comment(s) |
|---|
- This family of enzymes includes most of the bacterial tyrosine
kinases.
- These enzymes do not share sequence or structural homology with
eukaryotic tyrosine kinases, and exploit ATP/GTP-binding Walker
motifs to catalyze autophosphorylation and substrate phosphorylation
on tyrosine.
- Two subfamilies have been defined: P-type enzymes contain an
N-terminal transmembrane portion and an extracellular hairpin loop
domain. The intracellular portion comprises the catalytic domain and
a tyrosine-rich C-terminal domain that contains the site for
autophosphorylation.
- In F-type enzymes the extracellular transmembrane domain and the
intracellular catalytic domain are two independent proteins encoded
by two separate genes.
- The majority of characterized bacterial tyrosine kinases regulate the
production and export of capsular and extracellular polysaccharides,
but other members are involved in many other functions.
|
| Cross-references |
|---|
| BRENDA | 2.7.10.3 |
| EC2PDB | 2.7.10.3 |
| ExplorEnz | 2.7.10.3 |
| KEGG Ligand Database for Enzyme Nomenclature | 2.7.10.3 |
| IUBMB Enzyme Nomenclature | 2.7.10.3 |
| MEDLINE | Find literature relating to 2.7.10.3 |
| MetaCyc | 2.7.10.3 |
| Rhea expert-curated reactions | 2.7.10.3 |
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 2.7.10.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.7.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-
